Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.11.1.7 (peroxidase)
65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to investigate the existence of genetic variability in antioxidant enzyme defenses in sunflower, twelve inbred lines, six cytoplasmic male-sterile and six restorer lines, commonly used in breeding programs have been compared with respect to (a) their levels of constitutive superoxide dismutase (SOD, EC 1.15.1.1), catalase (CAT, EC 1.11.1.6), ascorbate peroxidase (APX, EC 1.11.1.11), glutathione reductase (GR, EC 1.6.4.2) and guaiacol-dependent peroxidase (GPX, EC 1.11.1.7), and (b) their isoenzyme polymorphism in SOD, CAT, and GPX activities. Constitutive levels of antioxidant enzymes in the 2nd leaf pair of 15-20-day-old sunflower plants showed significant differences between lines. The ranges of variation in enzyme activities of the different lines were equivalent to 34.3% (CAT), 38.2% (SOD), 59.5% (APX), 60.0% (GR), and 62.9% (GPX) of the respective maximal values. Isoenzyme profiles of CAT, GPX and SOD revealed the existence in sunflower of at least three, six and four isoforms of these enzymes, respectively. Further characterization of SOD isoenzymes revealed that no isoenzyme corresponded to a Mn-SOD, the faster moving isoform being a Cu/Zn-SOD and the remainder three Fe-SODs. Among the twelve inbred sunflower lines studied there were ample qualitative, and sometimes quantitative too, differences in isoenzyme dotation of CAT, GPX and Fe-SOD.
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PMID:Sunflower (Helianthus annuus) variability in antioxidant enzyme defenses. 1069 64

The response of both specific (ascorbate peroxidase, APX) and unspecific (POD) peroxidases and H(2)O(2) content of sunflower plants (Helianthus annuus L. cv. Hor) grown hydroponically with (C) or without (-Fe) iron in the nutrient solution were analysed to verify whether iron deficiency led to cell oxidative status. In -Fe leaves a significant increase of H(2)O(2) content was detected, a result confirmed by electron microscopy analysis. As regards extracellular peroxidases, while APX activity significantly decreased, no change was observed in either soluble guaiacol or syringaldazine-dependent POD activity following iron starvation. Moreover, guaiacol-dependent POD activity was found to decrease in both ionically and covalently-cell-wall bound fractions, while syringaldazine-POD activity decreased only in the covalently-bound fraction. At the intracellular level both guaiacol-POD and APX activities underwent a significant decrease. The overall reduction of peroxidase activity was confirmed by the electrophoretic separation of POD isoforms and, at the extracellular level, by cytochemical localization of peroxidases by diaminobenzidine staining. The electrophoretic separation, besides quantitative differences, also revealed quantitative changes, particularly evident for ionically and covalently-bound fractions. Therefore, in sunflower plants, iron deficiency seems to affect the different peroxidase isoenzymes to different extents and to induce a secondary oxidative stress, as indicated by the increased levels of H(2)O(2). However, owing to the almost completely lack of catalytic iron capable of triggering the Fenton reaction, iron-deficient sunflower plants are probably still sufficiently protected against oxidative stress.
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PMID:Iron deficiency differently affects peroxidase isoforms in sunflower. 1118 10

The reactivity of recombinant pea cytosolic ascorbate peroxidase (rAPX) towards H2O2, the nature of the intermediates and the products of the reaction have been examined using UV/visible and EPR spectroscopies together with HPLC. Compound I of rAPX, generated by reaction of rAPX with 1 molar equivalent of H2O2, contains a porphyrin pi-cation radical. This species is unstable and, in the absence of reducing substrate, decays within 60 s to a second species, compound I*, that has a UV/visible spectrum [lambda(max) (nm) = 414, 527, 558 and 350 (sh)] similar, but not identical, to those of both horseradish peroxidase compound II and cytochrome c peroxidase compound I. Small but systematic differences were observed in the UV/visible spectra of compound I* and authentic rAPX compound II, generated by reaction of rAPX with 1 molar equivalent H2O2 in the presence of 1 molar equivalent of ascorbate [lambda(max) (nm) = 416, 527, 554, 350 (sh) and 628 (sh)]. Compound I* decays to give a 'ferric-like' species (lambda(max) = 406 nm) that is not spectroscopically identical to ferric rAPX (lambda(max) = 403 nm) with a first order rate constant, k(decay)' = (2.7 +/- 0.3) x 10(-4) s(-1). Authentic samples of compound II evolve to ferric rAPX [k(decay) = (1.1 +/- 0.2) x 10(-3) s(-1)]. Low temperature (10 K) EPR spectra are consistent with the formation of a protein-based radical, with g values for compound I* (g parallel = 2.038, g perpendicular = 2.008) close to those previously reported for the Trp191 radical in cytochrome c peroxidase (g parallel = 2.037, g perpendicular = 2.005). The EPR spectrum of rAPX compound II was essentially silent in the g = 2 region. Tryptic digestion of the 'ferric-like' rAPX followed by RP-HPLC revealed a fragment with a new absorption peak near 330 nm, consistent with the formation of a hydroxylated tryptophan residue. The results show, for the first time, that rAPX can, under certain conditions, form a protein-based radical analogous to that found in cytochrome c peroxidase. The implications of these data are discussed in the wider context of both APX catalysis and radical formation and stability in haem peroxidases.
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PMID:Detection of a tryptophan radical in the reaction of ascorbate peroxidase with hydrogen peroxide. 1135 29

Chilling whole rice seedlings at 5 degrees C significantly increased the time needed to recover linear growth and reduced the subsequent linear rate of radicle growth. Subjecting nonchilled seedlings to a 45 degrees C heat shock for up to 20 min did not alter subsequent growth, whereas a 3 min heat shock was optimal in reducing growth inhibition caused by 2 days of chilling. The activity of five antioxidant enzymes [superoxide dismutase (EC 1.15.1.1), catalase (CAT; EC 1.11.1.6), ascorbate peroxidase (APX; EC 1.11.1.11), glutathione reductase (GR; EC 1.6.4.2), and guaiacol peroxidase (GPX; EC 1.11.1.7)] and DPPH (1,1-diphenyl-2-picrylhydrazyl)-radical scavenging activity were measured in heat-shocked and/or chilled radicles. Heat shock slightly increased the activity of CAT, APX, and GR and suppressed the increase of GR and GPX activity during recovery from chilling. Increased CAT, APX, GR, and DPPH-radical scavenging activity and protection of CAT activity during chilling appear to be correlated with heat shock-induced chilling tolerance.
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PMID:Antioxidant enzymes and DPPH-radical scavenging activity in chilled and heat-shocked rice (Oryza sativa L.) seedlings radicles. 1180 22

Cucumber seedling radicles become more chilling sensitive as they elongate. Chilling seedlings with radicles 20 mm long for 48 h at 2.5 degrees C inhibited subsequent growth by 36%, while it reduced the growth of 70 mm-long radicles by 63%. Although the growth rate of non-chilled cucumber radicles at 25 degrees C is constant from 20 to 80 mm, tissue viability [i.e. reduction of TTC (2,3,5-triphenyltetrazolium chloride) to formazan] and DPPH (alpha,alpha-diphenyl-beta-picrylhydrazyl) radical scavenging activity of apical tissue declines as radicles elongate from 20 to 80 mm in length. TTC reduction, DPPH-radical scavenging activity and protein content of apical tissue were higher in 20 than in 70 mm radicles immediately after chilling and after an additional 48 h of growth at 25 degrees C. Catalase (CAT; EC 1.11.1.6) and ascorbate peroxidase (APX; EC 1.11.1.11) activity was higher in the apical tissue of 20 than in 70 mm radicles before chilling. Immediately after chilling and after an additional 48 h at 25 degrees C, superoxide dismutase (SOD; EC 1.15.1.1), glutathione reductase (GR; EC 1.6.4.2), and guaiacol peroxidase (GPX; EC 1.11.1.7) activity increased more rapidly in 70 mm radicles than in 20 mm radicles (SOD, GR, and GPX activity in 70 mm radicles was 1.5-, 1.9- and 8.6-fold higher, respectively, than in 20 mm radicles). However, APX and CAT activity in 20 mm radicles were always higher than in 70 mm radicles. Growth after chilling enhanced the activity of all antioxidant enzymes compared to that found in non-chilled tissue; however, CAT activity in 70 mm radicles did not recover to levels found in non-chilled tissue. Higher levels of CAT, APX and DPPH-radical scavenging activity are correlated with higher chilling tolerance of 20 mm-long cucumber radicles compared to 70 mm-long radicles.
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PMID:Reduced chilling tolerance in elongating cucumber seedling radicles is related to their reduced antioxidant enzyme and DPPH-radical scavenging activity. 1206 Feb 42

Our previous study suggests that salicylic acid mediates tolerance in barley plants to paraquat (Ananieva et al. 2002). To further define the role of SA in paraquat induced responses, we analysed the capacity of the antioxidative defence system by measuring the activities of several antioxidative enzymes: superoxide dismutase (SOD, EC 1.15.1.1), ascorbate peroxidase (APX, EC 1.11.1.11), glutathione reductase (GR, EC 1.6.4.2), dehydroascorbate reductase (DHAR, EC 1.8.5.1), catalase (CAT, EC 1.11.1.6), and guaiacol peroxidase (POX, EC 1.11.1.7). Twelve-day-old barley seedlings were supplied with 500 micromol/L SA or 10 micromol/L Pq via the transpiration stream and kept in the dark for 24 h. Then they were exposed to 100 micromol m(-2) s(-1) PAR and samples were taken 6 h after the light exposure. Treatment of seedlings with 10 micromol/L Pq reduced the activity of APX and GR, did not affect the activity of POX and DHAR but caused over a 40% increase in the activity of CAT. Pre-treatment with 500 micromol/L SA for 24 h in the dark before Pq application increased the activities of the studied enzymes in both the chloroplasts (SOD activity) and the other compartments of the cell (POX, CAT activity). The effect of SA pre-treatment was highly expressed on DHAR and POX activity. The data suggest that SA antagonizes Pq effects, via elicitation of an antioxidative response in barley plants.
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PMID:Exogenous treatment with salicylic acid leads to increased antioxidant capacity in leaves of barley plants exposed to paraquat. 1507 30

Tobacco (Nicotiana tabacum L. cv. Petit Havana) callus cultures were exposed to UV-C high dose pulse-treatment (254 nm, 50 kJ m(-2), 1 h-treatment). After 6, 24 and 48 h from the end of the treatment, calli were cut transversally in two layers and oxidative damage (malondialdehyde [MDA] and hydrogen peroxide), non-enzymatic (radical scavenging antioxidants [RSA] and polyamines) and enzymatic antioxidants (ascorbate peroxidase [APX, EC 1.11.1.11], glutathione reductase [GR, EC 1.6.4.2], catalase [CAT, EC 1.11.1.6] and guaiacol peroxidase [GPX, EC 1.11.1.7]) were evaluated. At each time-point data referred to UV-C treated calli were compared to data of untreated ones (control). Despite of a strong increase of H2O2 content, a slight cellular damage was observed in both upper and lower layers 24 and 48 h after UV-C treatment. An activation first of non-enzymatic antioxidants and then of enzymatic antioxidants was detected in UV-C treated calli. In particular, RSA and putrescine (PUT) accumulated 6 h after UV-C treatment while APX, GR and GPX enzyme activities increased 24 h after UV-C irradiation. Catalase activity did not change. UV-C-induced oxidative stress and antioxidative response were observed also in cell layers not directly exposed to UV irradiation, indicating that a stress signal was transmitted to the whole mass of callus.
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PMID:Spread of oxidative damage and antioxidative response through cell layers of tobacco callus after UV-C treatment. 1519 49

Ascorbate peroxidase is a bifunctional peroxidase that catalyzes the H(2)O(2)-dependent oxidation of both ascorbate and various aromatic substrates. The ascorbate binding site was recently identified as being close to the gamma-heme edge [Sharp, K. H., Mewies, M., Moody, P. C. E., and Raven, E. L. (2003)Nat. Struct. Biol. 10, 303-307]. In this work, the X-ray crystal structure of recombinant soybean cytosolic ascorbate peroxidase (rsAPX) in complex with salicylhydroxamic acid (SHA) has been determined to 1.46 A. The SHA molecule is bound close to the delta-heme edge in a cavity that connects the distal side of the heme to the surface of the protein. There are hydrogen bonds between the phenolic hydroxide of the SHA and the main chain carbonyl of Pro132, between the carbonyl oxygen of SHA and the side chain guanadinium group of Arg38, and between the hydroxamic acid group and the indole nitrogen of Trp41. The structure provides the first information about the location of the aromatic binding site in ascorbate peroxidase and, together with our previous data [Sharp, K. H., et al. (2003) Nat. Struct. Biol. 10, 303-307], completes the structural description of the binding properties of ascorbate peroxidase. The mechanistic implications of the results are discussed in terms of our current understanding of how APX catalyzes oxidation of different types of substrates bound at different locations.
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PMID:Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex. 1523 72

To gain a better insight into long-term salt-induced oxidative stress, some physiological parameters in marigold (Calendula officinalis L.) under 0, 50 and 100 mM NaCl were investigated. Salinity affected most of the considered parameters. High salinity caused reduction in growth parameters, lipid peroxidation and hydrogen peroxide accumulation. Under high salinity stress, a decrease in total glutathione and an increase in total ascorbate (AsA + DHA), accompanied with enhanced glutathione reductase (GR, EC 1.6.4.2) and ascorbate peroxidase (APX, EC 1.11.1.11) activities, were observed in leaves. In addition, salinity induced a decrease in superoxide dismutase (SOD, EC 1.15.1.1) and peroxidase (POX, EC 1.11.1.7) activities. The decrease in dehydroascorbate reductase (DHAR, EC 1.8.5.1) and monodehydroascorbate reductase (MDHAR, EC 1.6.5.4) activities suggests that other mechanisms play a major role in the regeneration of reduced ascorbate. The changes in catalase (CAT, EC 1.11.1.6) activities, both in roots and in leaves, may be important in H2O2 homeostasis.
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PMID:Antioxidative responses of Calendula officinalis under salinity conditions. 1547 74

Twelve-day-old seedlings of pea (Pisum sativum L.) that were treated for 4 days by 20 and 100 micromol/l Cd(NO3)2 or CuSO4 showed a growth reduction in all organs. From root protein extracts, the activities of guaiacol peroxidase (GPX; EC 1.11.1.7), ascorbate peroxidase (APX; EC 1.11.1.11), coniferyl alcohol peroxidase (CAPX), NADH oxidase, and indole-3-acetic acid (IAA) oxidase were measured in covalently--and ionically--[symbol: see text] bound cell wall, soluble, and microsomal membrane fractions. With the exception of 20 micromol/l Cu, metal treatments enhanced GPX activity in all fractions. Only IAA oxidase activity was metal-elevated in the covalently bound cell wall fraction, while the ionic one showed Cd stimulation for all assayed enzymic activities. These effects were not entirely observed in Cu-treated plants, since APX and IAA oxidase activities were only enhanced in this fraction. However, soluble extract showed stimulation of APX activity, while in the microsomal fraction metal exposure also increased the activities of CAPX and NADH oxidase. Differential responses of root cell fractions to the presence of cadmium and copper ions are discussed in regard to the contribution of their enzymic capacities in antioxidant, lignification, and auxin degradation pathways. Comparisons between metals and dose effects are also underlined.
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PMID:Effects of cadmium and copper on peroxidase, NADH oxidase and IAA oxidase activities in cell wall, soluble and microsomal membrane fractions of pea roots. 1560 14


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